5H2P
A three dimensional movie of structural changes in bacteriorhodopsin: structure obtained 657 us after photoexcitation
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005216 | molecular_function | monoatomic ion channel activity |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0006811 | biological_process | monoatomic ion transport |
| A | 0007602 | biological_process | phototransduction |
| A | 0009881 | molecular_function | photoreceptor activity |
| A | 0016020 | cellular_component | membrane |
| A | 0050896 | biological_process | response to stimulus |
| A | 1902600 | biological_process | proton transmembrane transport |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 13 |
| Details | binding site for residue RET A 301 |
| Chain | Residue |
| A | TRP86 |
| A | PRO186 |
| A | TRP189 |
| A | ASP212 |
| A | LYS216 |
| A | THR89 |
| A | THR90 |
| A | LEU93 |
| A | MET118 |
| A | TRP138 |
| A | SER141 |
| A | TRP182 |
| A | TYR185 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue L2P A 302 |
| Chain | Residue |
| A | ALA44 |
| A | LEU48 |
| A | PHE54 |
| A | THR107 |
| A | TYR147 |
| A | D10304 |
| site_id | AC3 |
| Number of Residues | 1 |
| Details | binding site for residue TRD A 303 |
| Chain | Residue |
| A | LEU149 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | binding site for residue D10 A 304 |
| Chain | Residue |
| A | LEU22 |
| A | L2P302 |
| A | HP6305 |
| site_id | AC5 |
| Number of Residues | 1 |
| Details | binding site for residue HP6 A 305 |
| Chain | Residue |
| A | D10304 |
| site_id | AC6 |
| Number of Residues | 2 |
| Details | binding site for residue OCT A 306 |
| Chain | Residue |
| A | LYS172 |
| A | ASN176 |
| site_id | AC7 |
| Number of Residues | 1 |
| Details | binding site for residue OCT A 307 |
| Chain | Residue |
| A | MYS308 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | binding site for residue MYS A 308 |
| Chain | Residue |
| A | ILE191 |
| A | OCT307 |
| A | L2P310 |
| site_id | AC9 |
| Number of Residues | 1 |
| Details | binding site for residue UND A 309 |
| Chain | Residue |
| A | L2P310 |
| site_id | AD1 |
| Number of Residues | 5 |
| Details | binding site for residue L2P A 310 |
| Chain | Residue |
| A | TYR131 |
| A | TRP138 |
| A | ILE203 |
| A | MYS308 |
| A | UND309 |
| site_id | AD2 |
| Number of Residues | 13 |
| Details | binding site for residue L2P A 311 |
| Chain | Residue |
| A | ILE52 |
| A | MET56 |
| A | TYR64 |
| A | TRP80 |
| A | ALA84 |
| A | PHE88 |
| A | GLY116 |
| A | ILE117 |
| A | GLY120 |
| A | LEU123 |
| A | LEU123 |
| A | VAL124 |
| A | C14314 |
| site_id | AD3 |
| Number of Residues | 1 |
| Details | binding site for residue MYS A 312 |
| Chain | Residue |
| A | TYR26 |
| site_id | AD4 |
| Number of Residues | 1 |
| Details | binding site for residue DD9 A 313 |
| Chain | Residue |
| A | ARG225 |
| site_id | AD5 |
| Number of Residues | 4 |
| Details | binding site for residue C14 A 314 |
| Chain | Residue |
| A | LEU87 |
| A | PRO91 |
| A | LEU95 |
| A | L2P311 |
| site_id | AD6 |
| Number of Residues | 1 |
| Details | binding site for residue OCT A 315 |
| Chain | Residue |
| A | TYR26 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 41 |
| Details | TOPO_DOM: Extracellular => ECO:0000269|PubMed:10452895, ECO:0000269|PubMed:28008064, ECO:0007744|PDB:1C3W |
| Chain | Residue | Details |
| A | GLN1-GLU9 | |
| A | GLY63-TYR79 | |
| A | THR128-ARG134 | |
| A | GLY192-ILE203 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 19 |
| Details | TRANSMEM: Helical; Name=Helix A => ECO:0000269|PubMed:10452895, ECO:0000269|PubMed:28008064, ECO:0007744|PDB:1C3W |
| Chain | Residue | Details |
| A | TRP10-VAL29 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 40 |
| Details | TOPO_DOM: Cytoplasmic => ECO:0000269|PubMed:10452895, ECO:0000269|PubMed:28008064, ECO:0007744|PDB:1C3W |
| Chain | Residue | Details |
| A | LYS30-TYR43 | |
| A | LEU97-THR107 | |
| A | GLY155-LYS172 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 18 |
| Details | TRANSMEM: Helical; Name=Helix B => ECO:0000269|PubMed:10452895, ECO:0000269|PubMed:28008064, ECO:0007744|PDB:1C3W |
| Chain | Residue | Details |
| A | ALA44-LEU62 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 16 |
| Details | TRANSMEM: Helical; Name=Helix C => ECO:0000269|PubMed:10452895, ECO:0000269|PubMed:28008064, ECO:0007744|PDB:1C3W |
| Chain | Residue | Details |
| A | TRP80-ASP96 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 19 |
| Details | TRANSMEM: Helical; Name=Helix D => ECO:0000269|PubMed:10452895, ECO:0000269|PubMed:28008064, ECO:0007744|PDB:1C3W |
| Chain | Residue | Details |
| A | ILE108-LEU127 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 19 |
| Details | TRANSMEM: Helical; Name=Helix E => ECO:0000269|PubMed:10452895, ECO:0000269|PubMed:28008064, ECO:0007744|PDB:1C3W |
| Chain | Residue | Details |
| A | PHE135-PHE154 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 18 |
| Details | TRANSMEM: Helical; Name=Helix F => ECO:0000269|PubMed:10452895, ECO:0000269|PubMed:28008064, ECO:0007744|PDB:1C3W |
| Chain | Residue | Details |
| A | VAL173-ILE191 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 19 |
| Details | TRANSMEM: Helical; Name=Helix G => ECO:0000269|PubMed:10452895, ECO:0000269|PubMed:28008064, ECO:0007744|PDB:1C3W |
| Chain | Residue | Details |
| A | GLU204-LEU223 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 1 |
| Details | SITE: Primary proton acceptor => ECO:0000305|PubMed:10903866, ECO:0000305|PubMed:10949309, ECO:0000305|PubMed:28008064 |
| Chain | Residue | Details |
| A | ASP85 |
| site_id | SWS_FT_FI11 |
| Number of Residues | 1 |
| Details | MOD_RES: Pyrrolidone carboxylic acid => ECO:0000269|PubMed:9541408 |
| Chain | Residue | Details |
| A | GLN1 |
| Chain | Residue | Details |
| A | LYS216 |
